ID   LCF3_YEAST              Reviewed;         694 AA.
AC   P39002; D6VVS1;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 189.
DE   RecName: Full=Long-chain-fatty-acid--CoA ligase 3;
DE            EC=6.2.1.3 {ECO:0000269|PubMed:8206942};
DE   AltName: Full=Fatty acid activator 3;
DE   AltName: Full=Long-chain acyl-CoA synthetase 3;
GN   Name=FAA3; OrderedLocusNames=YIL009W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   PubMed=8027063; DOI=10.1016/s0021-9258(17)32414-6;
RA   Johnson D.R., Knoll L.J., Rowley N., Gordon J.I.;
RT   "Genetic analysis of the role of Saccharomyces cerevisiae acyl-CoA
RT   synthetase genes in regulating protein N-myristoylation.";
RL   J. Biol. Chem. 269:18037-18046(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169870;
RA   Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA   Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA   Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA   Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA   Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL   Nature 387:84-87(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=8206942; DOI=10.1016/s0021-9258(17)34014-0;
RA   Knoll L.J., Johnson D.R., Gordon J.I.;
RT   "Biochemical studies of three Saccharomyces cerevisiae acyl-CoA
RT   synthetases, Faa1p, Faa2p, and Faa3p.";
RL   J. Biol. Chem. 269:16348-16356(1994).
RN   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [7]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH FRK1.
RX   PubMed=20489023; DOI=10.1126/science.1176495;
RA   Breitkreutz A., Choi H., Sharom J.R., Boucher L., Neduva V., Larsen B.,
RA   Lin Z.Y., Breitkreutz B.J., Stark C., Liu G., Ahn J., Dewar-Darch D.,
RA   Reguly T., Tang X., Almeida R., Qin Z.S., Pawson T., Gingras A.C.,
RA   Nesvizhskii A.I., Tyers M.;
RT   "A global protein kinase and phosphatase interaction network in yeast.";
RL   Science 328:1043-1046(2010).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Activates endogenous long-chain fatty acids (LCFA) by
CC       esterification of the fatty acids into metabolically active CoA-
CC       thioesters for subsequent degradation or incorporation into
CC       phospholipids (PubMed:8206942). Acts preferentially on C16 and C18
CC       fatty acids with a cis-double bond at C-9-C-10 (PubMed:8206942).
CC       {ECO:0000269|PubMed:8206942}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-
CC         CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560,
CC         ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3;
CC         Evidence={ECO:0000269|PubMed:8206942};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoate + ATP + CoA = (9Z)-octadecenoyl-CoA + AMP +
CC         diphosphate; Xref=Rhea:RHEA:33607, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:30823, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57387, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000269|PubMed:8206942};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33608;
CC         Evidence={ECO:0000305|PubMed:8206942};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + hexadecanoate = AMP + diphosphate + hexadecanoyl-
CC         CoA; Xref=Rhea:RHEA:30751, ChEBI:CHEBI:7896, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:8206942};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752;
CC         Evidence={ECO:0000305|PubMed:8206942};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-hexadecenoate + ATP + CoA = (9Z)-hexadecenoyl-CoA + AMP +
CC         diphosphate; Xref=Rhea:RHEA:33647, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:32372, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:61540, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000269|PubMed:8206942};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33648;
CC         Evidence={ECO:0000305|PubMed:8206942};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-tetradecenoate + ATP + CoA = (9Z)-tetradecenoyl-CoA + AMP
CC         + diphosphate; Xref=Rhea:RHEA:33643, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:32370, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:65060, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000269|PubMed:8206942};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33644;
CC         Evidence={ECO:0000305|PubMed:8206942};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z,12Z)-octadecadienoate + ATP + CoA = (9Z,12Z)-
CC         octadecadienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:33651,
CC         ChEBI:CHEBI:30245, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000269|PubMed:8206942};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33652;
CC         Evidence={ECO:0000305|PubMed:8206942};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P30624};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.7. {ECO:0000269|PubMed:8206942};
CC       Temperature dependence:
CC         Optimum temperature is 25 degrees Celsius.
CC         {ECO:0000269|PubMed:8206942};
CC   -!- SUBUNIT: Interacts with FRK1. {ECO:0000269|PubMed:20489023}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14562095}.
CC   -!- DOMAIN: The FACS motif is required for catalytic activity and substrate
CC       specificity. {ECO:0000250|UniProtKB:P30624}.
CC   -!- MISCELLANEOUS: Present with 6440 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; Z29647; CAA82755.1; -; Genomic_DNA.
DR   EMBL; Z38113; CAA86241.1; -; Genomic_DNA.
DR   EMBL; AY558110; AAS56436.1; -; Genomic_DNA.
DR   EMBL; BK006942; DAA08537.1; -; Genomic_DNA.
DR   PIR; B54901; B54901.
DR   RefSeq; NP_012257.1; NM_001179359.1.
DR   AlphaFoldDB; P39002; -.
DR   SMR; P39002; -.
DR   BioGRID; 34983; 67.
DR   DIP; DIP-4210N; -.
DR   IntAct; P39002; 8.
DR   MINT; P39002; -.
DR   STRING; 4932.YIL009W; -.
DR   SwissLipids; SLP:000001033; -.
DR   iPTMnet; P39002; -.
DR   MaxQB; P39002; -.
DR   PaxDb; 4932-YIL009W; -.
DR   PeptideAtlas; P39002; -.
DR   EnsemblFungi; YIL009W_mRNA; YIL009W; YIL009W.
DR   GeneID; 854808; -.
DR   KEGG; sce:YIL009W; -.
DR   AGR; SGD:S000001271; -.
DR   SGD; S000001271; FAA3.
DR   VEuPathDB; FungiDB:YIL009W; -.
DR   eggNOG; KOG1180; Eukaryota.
DR   GeneTree; ENSGT00940000171609; -.
DR   HOGENOM; CLU_000022_45_2_1; -.
DR   InParanoid; P39002; -.
DR   OMA; KIFQWAA; -.
DR   OrthoDB; 443463at2759; -.
DR   BioCyc; YEAST:YIL009W-MONOMER; -.
DR   Reactome; R-SCE-434313; Intracellular metabolism of fatty acids regulates insulin secretion.
DR   Reactome; R-SCE-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR   BioGRID-ORCS; 854808; 3 hits in 10 CRISPR screens.
DR   PRO; PR:P39002; -.
DR   Proteomes; UP000002311; Chromosome IX.
DR   RNAct; P39002; Protein.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005811; C:lipid droplet; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:SGD.
DR   GO; GO:0031957; F:very long-chain fatty acid-CoA ligase activity; IDA:SGD.
DR   GO; GO:0001676; P:long-chain fatty acid metabolic process; IGI:SGD.
DR   GO; GO:0035336; P:long-chain fatty-acyl-CoA metabolic process; IBA:GO_Central.
DR   CDD; cd17639; LC_FACS_euk1; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   PANTHER; PTHR43272:SF83; ACYL-COA SYNTHETASE LONG-CHAIN, ISOFORM J; 1.
DR   PANTHER; PTHR43272; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cell membrane; Fatty acid metabolism; Ligase;
KW   Lipid metabolism; Magnesium; Membrane; Nucleotide-binding;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..694
FT                   /note="Long-chain-fatty-acid--CoA ligase 3"
FT                   /id="PRO_0000193121"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           527..576
FT                   /note="FACS"
FT                   /evidence="ECO:0000250|UniProtKB:P30624"
FT   BINDING         269..280
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P69451"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
SQ   SEQUENCE   694 AA;  77947 MW;  7AB33044335A5295 CRC64;
     MSEQHSVAVG KAANEHETAP RRNVRVKKRP LIRPLNSSAS TLYEFALECF NKGGKRDGMA
     WRDVIEIHET KKTIVRKVDG KDKSIEKTWL YYEMSPYKMM TYQELIWVMH DMGRGLAKIG
     IKPNGEHKFH IFASTSHKWM KIFLGCISQG IPVVTAYDTL GESGLIHSMV ETESAAIFTD
     NQLLAKMIVP LQSAKDIKFL IHNEPIDPND RRQNGKLYKA AKDAINKIRE VRPDIKIYSF
     EEVVKIGKKS KDEVKLHPPE PKDLACIMYT SGSISAPKGV VLTHYNIVSG IAGVGHNVFG
     WIGSTDRVLS FLPLAHIFEL VFEFEAFYWN GILGYGSVKT LTNTSTRNCK GDLVEFKPTI
     MIGVAAVWET VRKAILEKIS DLTPVLQKIF WSAYSMKEKS VPCTGFLSRM VFKKVRQATG
     GHLKYIMNGG SAISIDAQKF FSIVLCPMII GYGLTETVAN ACVLEPDHFE YGIVGDLVGS
     VTAKLVDVKD LGYYAKNNQG ELLLKGAPVC SEYYKNPIET AVSFTYDGWF RTGDIVEWTP
     KGQLKIIDRR KNLVKTLNGE YIALEKLESV YRSNSYVKNI CVYADESRVK PVGIVVPNPG
     PLSKFAVKLR IMKKGEDIEN YIHDKALRNA VFKEMIATAK SQGLVGIELL CGIVFFDEEW
     TPENGFVTSA QKLKRREILA AVKSEVERVY KENS
//